My Kingdom for a Mitochondrial DNA Test!

Richard III really did not have a good life.

Or, at least, that's the way historians have painted it. Vilified as the last king of the House of York, as the object of satire in Shakespeare's play Richard III, and as the man who plead, "My kingdom for a horse!", King Richard III proves that history is not kind to those on the losing side of war. The possible discovery of his remains in a parking lot only goes to further desecrate his memory (the poor man).

Killed at the Battle of Bosworth, the final, monumental battle between the Houses York and Lancaster in the War of the Roses, Richard III is famously remembered as the deformed, villainous king who seized the throne after his brother's death and killed the remaining heirs, his young nephews, to ensure his reign. Only lasting two years, his reign marked the end of the House of York, proving once again that you should never kill your family relations if you want your lineage to remain on the throne. (Come on, Richard). Although his remains were buried at a Greyfriar's friary, time had since destroyed the church, and the known location of Richard III's unmarked grave had been lost to history.

Until a group of people decided that it was a brilliant idea to look underneath a Leicester parking lot. No, really. Recently, archeologists had discovered the remains of an individual who was theorized to the infamous king of the 15th century. Although the skeleton showed signs of scoliosis (which Richard III was afflicted with) and battle injuries to the skull and spine (injuries that were also reportedly what killed the king), researchers needed more concrete evidence to ensure that the body really was the infamous king. Which is why they turned to radiocarbon dating and mitochondrial DNA testing to prove that the remains were truly those of Richard III.

Radiocarbon dating is specifically geared towards determining the how much time has passed since an organic organism died. Radiocarbon dating measures the ratio of carbon-14 to carbon-12. While an organism is living, it absorbs the carbon-14 and carbon-12 in the atmosphere into their system. When the organism dies, however, it retains the carbon-12 in its system, as carbon-12 is a stable isotope, but gradually begins to lose the carbon-14, as it is a radioactive isotope and degrades over time. Because the half-life of carbon-14 is known, the amount of carbon-14 lost in a dead organism (found by comparing the ratio of carbon-12 to carbon-14) can tell the researcher how long the organism has been dead. Radiocarbon dating of the skeletal remains found in the parking lot show that they were from an individual who died between 1455 and 1540, a range that encompasses the time of death of Richard III.

A time range, however, is hardly enough to conclusively determine if the skeleton was the real deal.  To be able to determine whether the poor guy was the notorious 15th century king, the researchers at Leicester used mitochondrial DNA to test for a DNA match to the later relations of the king. (And this is where archaeological research begins to sound more and more like a paternity test.) Mitochondrial DNA analysis is basically the same as any other DNA analysis, except the researcher sequences the genome of the mitochondrial DNA instead of the traditional, nucleus DNA. The primary reason for sequencing mitochondrial DNA is simply because of the amount of DNA available to sequence. In a cell there are hundreds of mitochondria to one nucleus. Not only is it easier to find mitochondrial DNA than it is to find nuclear DNA, the degradation of the skeletal specimen Leicester researchers found makes it even more necessary to find enough DNA that had not degraded over time to be used in the analysis.

With the sequencing of the mitochondrial DNA (which basically means they mapped out all of the DNA nucleotides and determined the specific order each of them) they then compared them to the mitochondrial DNA sequences of known relatives to the lost king. The relatives, which include Canadian carpenter Michael Ibsen and a confirmed anonymous descendant, prove "beyond reasonable doubt" that the genomic sequences match and that the skeletal remains are those of a relative to the two Richard III decedents. By simple deduction and process of elimination, the conclusion is obvious.

Yeah! The mystery is solved! We can go home!

But who really wants to go home? As Dr. Turi King, from University of Leicester, said, "It is an extremely rare occurrence that archaeologists are involved in the excavation of a known individual, let alone a king of England...Sequencing the genome of Richard III is a hugely important project that will help to teach us not only about him, but ferment discussion about how our DNA informs our sense of identity, our past and our future." In other words, the genomic details of Richard III's DNA will allow us to know several key aspects to his genetic make-up, such as his hair color, his eye color, and how easily he contracted diseases. His DNA will allow researchers (and avid readers like us) to take a quick glimpse into the past and see how his genetic ancestry could have possibly affected the modern population, and if any other organisms, such as pathogens, decided to snuggle in with Richard III's DNA and make a new home.

Although Shakespeare described Richard III as a man who "clothe [his] naked villainy /  With odd old ends, stol’n out of holy writ / And seem a saint, when most [he] play the devil," the physical man leaves remarkable DNA and materials that prove to be a godsend to both historians and archaeologists alike. Whether the man truly uttered the words "My kingdom for a horse!" we know now that the man lived and ate and breathed just like us all (aside from the fact that he was the ruler of England and we all, presumably, are not), and the discovery of his remains truly breathes new insight and information into the history that we all know and love.
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My name is Diana. I’m a pianist, a snail lover, and a lock-pick smith in training. 

What the "Frack"?

Few topics in modern chemistry and environmental science have been as polemical as fracking. Ask anyone well versed in drilling, environmental activism, or alternative energy, and you are sure to hear his or her passionate (read: loud) opinion. The rest of us, who are perhaps less literate in these topics, have certainly heard the buzzword before, and are familiar with the heated debate it prompts.

Whether you know what fracking is or not, you definitely know that people either love it or hate it. However, before newcomers can fully form their opinion, they often get lost in the chemical jargon.

So, what the “frack” is fracking anyway?

“Fracking” refers to hydraulic fracturing, a process of removing natural gas and oil from the ground. Fracking is often proposed as an alternative to traditional extraction methods, such as oilrigs. The process is as follows:

First, “fracturing fluids”, made of water and sand, are pushed into the ground at high pressures. The force fissures the ground, and frees the natural resources from the rocks below. This process takes place deep in the earth’s crust, no less than 7,000 feet below.

Once free, the resources travel horizontally, meet a deep vertical well, and move upwards to the surface casing, a large steel pipe. The surface casing preserves the groundwater from natural gas related contamination, and move the resources towards the purification center. At the purification center they are processed and prepared for distribution and consumption.

 Sounds great, right?

Well, not everyone thinks so. Much of the scrutiny of fracking, particularly from an environmental lens, points towards the possibility of contamination and the potentially dangerous repercussions on surrounding land.

For example, fracking plants have a tendency to increase downstream pollution, sometimes up to 200 times more radioactivity due to fracking by-products. Looking beyond surface water, contamination due to “fracturing liquids” exposure is a serious issue as well. The chemicals that make up “0.5-2.0 percent” of the solution used to fissure the ground can be very dangerous. If this mixture is not pressurized out of the ground properly, it can lead to serious ground water contamination and may alter crop growth.

However, do these issues nail the coffin for fracking completely?

No, and here’s why: Fracking is a great way to utilize otherwise inaccessible natural gas and resources to stabilize our energy consumption needs. For one, the streamlining of the gas flow from the rig to the well is highly economical. Instead of having to construct several heavy duty, expensive rigs in many places, fracking allows for a greater field of resources to be plucked from the ground, without superfluous construction.

Further, in terms of global energy issues, fracking may be the answer that the United States, and other severely petroleum dependent countries, needs to wean itself off of Middle-Eastern resource reliance. The increase in job availability and promotion of local fuel development might just be the economic push the US needs in these trying times, with a potential 1.6 million new jobs in the next 20 years.

Nor does fracking mean environmental ignorance in favor of economic stability. A recent study from the City Journal suggests that fracking may reap environmental benefits as well. For example, shale is significantly cleaner than coal, and emits fewer green house gases. In fact, the greater prevalence of natural gas use is most likely the source of the drop in America’s greenhouse gas emissions by “5.3 percent” from 2011 to 2012.

Sure, fracking is not perfect and should not be treated as such. However, through the current reality of quickly depleting energy sources and overt foreign dependency, fracking may be the only viable, consistent, and environmentally friendly alternative to oil at this time.

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Hi! I’m Sonia, a DCDS grad who will be attending UMich in the Fall.( Go Blue!) I love to travel, play soccer, and read at least 3 books simultaneously. Excited for the future, I hope to study biology and/or environmental science. 

Keep Calm and Curry On.

Sophomore year, whenever the school cafeteria would serve chicken curry, I would run towards the lunch lines (the only running I ever did) while screaming like a toddler. My Indian friends would grin at each other as I engulfed my fourth helping of "buttered chicken."

“Patrick” they would say, “stop eating that trash”. Later I would learn that the school’s buttered chicken was an inferior imitation of authentic Indian buttered chicken, which is orange to yellow in color, compared to the sickly pale color of my school’s buttered chicken. Buttered chicken takes its color from turmeric, a spice native to Indian. Because of its vibrant color and tendency to stain, turmeric has been used historically as a dye. The compound Curcumin, shown below is responsible for its color.

Keto form of Curcumin

My good friend, Vivek Nair, further said that turmeric had disinfecting properties and has been used as a folk medicine in India for quite a while now. He gave an anecdote about how his grandmother would boil water, then sprinkle a dash of turmeric in it further help disinfect it. How does turmeric kill bacterial and viral infections? This remains unknown. Researchers are not certain if turmeric is even capable of disinfecting wounds. Perhaps Vivek is just a big, fat liar. Perhaps this is something worth investigating myself. It’s a shame that I’ll have to resort to self-testing as no one seems keen to me sprinkling orange power into their open wounds.

I did not discover until later while writing this blog that while turmeric may be incapable of disinfecting wounds, it has been found to inhibit the growth of V. parahaemolyticus, a bacterium found to cause gastrointestinal illness when ingested. Turmeric is also the most effective at inhibiting the growth of Helicobacter pylori, a similar bacterium that causes stomach illnesses.

While its disinfectant properties are uncertain, turmeric boasts a myriad of other medicinal properties. With its ability to reduce inflammation, treat digestive problems and hinder some cancers, I am tempted to label it as a wonder spice. However, the University of Maryland Medical center warns that some of these effects have not been tested in humans and that only cucurmin extracted from turmeric, not turmeric as a whole, has been used in these tests.  

In 2007, a group of researchers demonstrated that turmeric inhibits the growth of Vibrio parahaemolyticus, Bacillus cereus, Pseudomonas aeruginosa, and Proteus mirabilis all of which are histamine-producing bacteria. (Histamine is responsible for inflammation). However, I was disappointed to find out that cinnamon and clover are more effective at inhibiting the growth of such bacteria.

What about turmeric’s ability to combat cancer? Turmeric has been shown to decrease uncontrolled cell reproduction and to induce apoptosis (programmed cell death) in tumor cells. Mice injected with cancer cells were then treated with turmeric (10-40 grams). Researchers found that mice treated with turmeric experienced up to 80% less tumor formation than untreated mice.

 Cinnamon Turmeric Challenge

Hold on, hold on, you may say to yourself. “Self, is this turmeric substance really as good as this Patrick fellow says it is? If it’s so good, how comes it isn’t more popular?” The University of Maryland Medical Center suggests that long-termed consumption of turmeric may cause stomach upset. Turmeric also acts as a blood thinner and may lower blood sugar count. Before rushing off to the nearest supermarket to hoard turmeric, you should be advised that the turmeric from the store may contain some impurities.

Remember, when you’re eating butter chicken, you’re not getting fatter, you’re building immunity to cancer. 

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I'm Patrick. I'm young, and I have dreams and passions.

Shoo Mosquito, You Can’t Bother Me

The newest scientific breakthrough: invisibility…well, invisibility to mosquitos at least. This new discovery in the chemistry sphere could eliminate a problem that has been, pardon the pun, bugging innocent kumbaya-singers and twilight pontoon cruisers around the globe for ages. We’ve all been there: sitting around the campfire at a summer powwow, enjoying a friendly conversation, when you are interrupted by a tingling…no…gradual itching sensation on your ankle. The worst part is that as much as you try to swat that little blood-sucker away, it always manages to find its way back. Talk about persistence.

Making humans invisible to mosquitos may seem like a daunting idea. To understand it better, it helps to be familiar with how the critters find their way to our elbows and ankles in the first place. Mosquitos follow carbon dioxide trails that waft away from all living organisms and can use these gaseous paths to sense a host up to 100 feet away. At a closer range, mosquitos use body heat to find and latch onto humans. This description might have you thinking that all they want is a warm hug, but don’t be fooled. Researchers have determined that hungry mosquitos use cpA neurons, olfactory cells located near their antennae, to track down hosts from distances exponentially larger than the little buggers themselves. Aside from the mosquito’s biology, secretion from your skin also helps the blood-feeders find their next meal. To determine which secreted chemicals mosquitos use to pinpoint hosts, scientists conducted an experiment where they sprayed different bodily substances in a cage chock full of the insects and inserted their own hands as bug bait. However unpleasant the process sounds, the results were worthwhile. In addition to other enticing chemicals, experts found that human sweat, mainly comprised of lactic acid, attracted almost 90% of the mosquitos. Sounds appetizing, right?

But, in all seriousness, the question still remains: how does one go about making themselves invisible to this seemingly inescapable summer pest? Dr. Ulrich Bernier, a chemist in the Mosquito and Fly Research Unit of the U.S. Department of Agriculture, is close to an answer. He has identified over 200 naturally occurring chemicals called attraction inhibitors on human skin that actually, if in a large enough concentration, prevent mosquitos from successfully locating a host. If they could be harnessed in substantial amounts, Dr. Bernier would have an amazingly effective bug spray on his hands, giving OFF!® a run for their money.

As close as research appears to improving the lives of campers, boaters and outdoorspeople everywhere, as of now solutions are still in the laboratory experimentation phase. With any luck, we can expect to be superheroes, invisible to those irksome mosquitos, in the near future. Until then, we’ll be itching with anticipation.

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My name is Leanna. I’m a horse rider, volleyball player and chemistry student!

Colors and Critters

Like many of my classmates, I feel the pressure of a second-generation teenager trying to fulfill my parents’ aspirations. I have to admit I’m pretty “white-washed,” but my Indian culture—from the spicy satisfaction of a crispy, golden samosa to seeing my groom ride in on a horse—holds a place dear to my heart. As a dancer, I love the colorful outfits most of all. 

I know that my grandmother’s neighbor’s sister’s gardener set us up with these silk dresses, but where did they really come from? To put it bluntly, they came from bugs. Silkworms. I refuse to share a room with a spider, but thank goodness for these little guys. Silkworms are just about three inches long and—fun fact—shed their skin five times as larvae. For over 5,000 years, they have been spinning cocoons for silk production. But these fibers are creamy white, and most of us want something more interesting. The energy consuming practice of dying silk externally creates so much toxin-filled wastewater that scientists have turned to a new method: feeding caterpillars dyed leaves. The silkworms are fed just before they start spinning and can then spin colored, rather than white cocoons. Pretty cool, right? Researchers in Pune and Mysore dipped mulberry leaves (their food) in azo dyes and found that three out of seven types of dyes transferred into the caterpillars’ silk and fortunately did not affect their growth.

Why did some dyes work, and others not? Basically, certain dyes dissolve better in water than others. If you want to get technical, it has to do with the hydrophobicity of the dye as it goes from the feed to silk fiber. Scientists look at how the coloring dissolves in a hydrophobic solvent like octanol (it has a phobia of water) to how well it dissolves in water itself. The more hydrophobic, oily molecules tend to show up in the silk because they aren’t easily cleared from the silkworm’s body. Hydrophilic (water loving) coloring molecules, on the other hand, are often dissolved out when the cocoons are dipped in water. Using the right dye can produce vibrant yellows, pinks, and greens without the dangers of external dying.

The bottom line here is that these ideas are pretty great—a greener way to make beautiful clothing. If research goes well, there will definitely be perks. When I get dolled up for an Indian wedding or shindig, I won’t have to feel guilty for killing some innocent fish. (Three dead pet goldfish are all a girl can take).

But wait, it gets even better. The super silk has healing powers too. Researchers in Singapore found that the feeding process may be used to create thread with antibacterial properties. Antimicrobial drugs can be transferred into the silk just like the dye, and slowly released through an implant. To be honest, I’m up for any way to avoid choking on another white pill during flu season. The possibilities are endless, really. The same researchers are now monitoring cancer cells by feeding silkworms cancer-fighting drugs.

New methods for cultivating colored silk certainly look promising. I have a new found appreciation for the stranger who makes my grandmother’s outfits—who will help make my dream wedding dress a reality. If you’re curious, look here.
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N^2: DCDS, 2014.  I will be attending the University of Pennsylvania in the fall. I like music, travelling, and chemistry.

Barking up the Right Tree

Why don’t Native Americans get headaches? No, this isn’t the opening to a politically incorrect joke, and the answer is actually quite simple: willow bark! Native Americans have long chewed the bark of willow trees as a remedy for headache and muscular pain. The same is true about ancient Egyptians and Greeks. Now, while many ancient remedies don’t have great success rates (cough bloodletting cough), willow bark has shown up in multiple cultures and has stood the test of time. This article talks about the role willow bark has played in both ancient civilizations and as well as in the life of plants. So, is there any truth to willow bark’s salutary effects?

There sure is! Willow bark (particularly that from the white willow tree) contains a substance called salacin. The prefix, sali-, even comes from the Latin word salix, meaning willow. When salacin is ingested, the human body converts it into a new compound called salicylic acid. For the full process on how the body converts salicin to salicylic acid, look here. Salicylic acid is one of the main constituents of acetylsalicylic acid, more commonly known as aspirin.

Salicylic Acid

Salicylic acid and aspirin have similar structures and similar effects on the body. Both help reduce inflammation and mitigate pain. Thus, chewing some willow bark and gulping down an aspirin are going to have comparable results. However, there are notable differences. The effects of willow bark have been reported to be much slower than those of aspirin. The effects of willow bark have also been shown to last longer. Both treatments can cause an upset stomach, but willow bark has been reported to cause this side effect less frequently.

Willow bark is definitely a viable treatment for minor aches and pains. However, the amount of salicylic acid you can get from willow bark is relatively low, and chewing willow bark or drinking willow tea means you have to deal with their bitter taste. If you need quick relief, or you’re just not in the mood for an attack on your taste buds, then aspirin is probably the way to go. But if you’re looking for a natural source of pain relief that has hard science backing it up, then willow bark is a pretty good option.

Just couple of warnings. If you intend to remove bark off a willow tree, try to avoid taking it off the main trunk if you can. I mean, causing permanent damage to a tree is no way to say thank you! Also, remember that taking willow bark is a lot like taking aspirin. If you are allergic to aspirin or are not able to take it, you shouldn’t be taking willow bark either. The University of Maryland Medical Center has info on the dosing and usage of willow bark and is a recommended read to those interested in willow bark as an herbal therapy. Despite the trouble of finding a willow tree, the flavor, and a couple of other issues, I think you’ll agree that when it comes down to it, willow bark is a lot better than its bite.

If you’re interested in making some willow bark tea yourself, check out this site for a nice, simple to follow recipe.

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My name's Vivek. I'm a mountain biker, a card player, and an aspiring scientist. I'm a Michigander and a dog lover. Enjoy the post!

The Un-Bee-Lievable Antibiotic Properties of Honey

We’ve all squeezed the stomach of that golden bear sometime in the last couple of months and watched that gluey, sweet liquid emerge, whether to make a dessert or to sweeten some tea. Yes, I’m talking about honey, the wonderful sweetener that bees make by buzzing from plant to plant collecting nectar. However, we seldom realize the wondrous properties of honey that extend past our taste buds: like medicine!

Honey has been documented in diverse ancient civilizations for its antimicrobial properties and as a treatment for wrapping wounds. Yet, the antibiotic nature of honey had not been fully appreciated until recent years. Reading about the antimicrobial tendencies of honey, here and here, I realized that honey is so much more than a cooking ingredient; it’s a miracle worker for wounds and infections!

As it turns out, honey has some peculiar qualities (although these vary with various types of bees) that specifically aid in its war on bacteria.

•  First, and probably the one that you and I are most thankful for, honey’s high sugar content and low water content lead to honey being hygroscopic (jargon for something’s tendency to absorb moisture). As a result, it hinders the growth of bacteria in open wounds by creating a hostile environment.
• Second, honey has a relatively acidic pH (~4) that inhibits bacterial growth. In other words, honey sends bacteria packing because they can’t handle the harsh (and ironically sweet) climate.
• Third, honey also naturally produces a substance that you would otherwise find in the brown bottle at your local pharmacy: hydrogen peroxide (H₂O₂). Hydrogen peroxide production in honey is initiated by an enzyme called glucose oxidase, put into honey by our good old friend the bee, when the honey becomes diluted (e.g. when you put it on a burn or cut).
• Fourth, honey also seems to have been specially crafted by our Apis friends to have some particular bacteria-fighting agents, such as a protein called bee defensin-1 or HMF (Hydroxymethylfurfural), which both inhibit particular metabolic functions of the bacteria.

So, at the end of the day, the honeybees end up getting the bad rap while we should be thanking them for giving us nature’s antibiotic. I mean, we all know what it feels like to get stung by a bee (personally I’ve been stung by three at the same time – it HURTS), but we should also realize the tradeoff; in recent studies, honey has actually been more effective than some common antibiotics used in hospitals at treated burn and open wounds. So while you may hate or resent that flying, striped coat, it might end up helping you recover from an injury, suppress a cough, or even sweeten your cup of tea.

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Mihir: I am a chemistry student and an avid sports fan and player. I watch several sports, though football (because I play) and baseball have to be my favorites. In football, I play on the offensive line and hope to possibly pursue a college career as well. This is my first time blogging, so I hope you enjoy!

Forget the Venison!

Well, hunting season just ended here in Michigan, and people from all over have stowed away their rifles and camouflage after a mediocre hunt. However, a few have captured that huge, prized buck they’ve been after for years. But before you take off that head and mount it on your wall, you may want to get something out of it first. That’s right, the antlers of that buck can be just as important as that juicy meat. I’m talking about a substance that’s becoming more popular –and controversial– now than ever before: deer antler spray.

Increasingly used nowadays, deer antler spray is quickly becoming one of the most popular and scrutinized supplement used by professional athletes. First used in China thousands of years ago for traditional medicine purposes, deer antler spray is now used by athletes in the U.S to help build and repair muscle.

An intricate process goes into creating the spray. While a male deer is growing up, its antlers grow very quickly, and produce a velvety texture on the outside. During this growing phase, some deer get their antlers clipped as to prevent them from getting too hard or sharp later on. When the tip is clipped off, it is then frozen, and sent to manufacturers who create the lucrative spray. “But wait,” you may ask, “what’s so special about the deer’s antlers that help athletes?” The answer lies in the chemical composition of the antlers themselves.

The main reason that deer antlers grow so quickly is that they contain a protein called IGF-1. IGF-1, or Insulin-like growth factor -1, is the same protein that exists in humans, and helps children grow. The protein helps create cells which can “generate new muscle after exercise-induced injury,” according to Business Insider. This process works because the brain’s growth hormone tells the liver to create IGF-1 (shown below), which “binds to the receptors in muscle cells, signaling them to multiply and grow,” according to CBS. When muscles are torn or strained, like NFL linebacker Ray Lewis’ triceps injury in 2012, deer antler spray can be (and is widely) used. Taken by mouth, the spray increases levels of IGF-1 in the body, so cells are created that can help heal damaged muscles faster and thus lead to a quicker recovery time.

IGF-1

Because of its capabilities, deer antler spray was banned by the World Anti-Doping Association. This treats IGF-1 as a performance enhancing drug, like testosterone or HGH. However, the ban was overturned when research showed that the deer antler sprays only contained small amounts of IGF-1. That research certainly didn’t stop athletes from using the product, however, as a supplement seller “Nutronics Labs” reported that hundreds of athletes continue to purchase and use the spray.

For now, deer antler spray is banned by some professional sports organizations, and is becoming more scrutinized as its popularity rockets. What do you think? Should deer antler spray be treated as another PED, or should it be given a little more leeway in locker rooms and training facilities? The “buck” stops here.
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Kiran

high school junior

basketball, food, and science enthusiast

En-gene-ering

"Okay I did the four in the first row, your turn."

I snapped out of my stupor and switched seats with my project partner and waited for my eyes to adjust to the blinding glare of the monitor he was working on. As my project partner and fellow intern and volunteer at Henry Ford Hospital's Neurology Research Department and I switched seats in the dark microscopy room, I had two thoughts. One was of how many more assays or cell samples we still needed to take pictures of and count the cells in. The other was of the implications of the data we were currently collecting from the samples we had spent two weeks preparing.

We sat in that dark room for hours, painstakingly adjusting settings on the microscope and counting the cells in each of our sample. When we weren't in this cramped room, hoping that no one would suddenly open the door and throw off the sensitive machine and ruin our images, we sat in front of a lab hood, dying cells with different indicators or watched as our lab mentor cared for the mice he was using for his projects. This went on for about six and a half weeks.

Fortunately, by the end of my internship, the bevy of tests we had performed on the four different samples of glioma cells yielded the results my partner and I had hoped for. For context, a glioma is a brain tumor known for its exceptionally destructive and invasive nature. Our project wanted to figure out if there is a more effective form of treatment for the tumor than what currently exists. Currently, patients who have glioma have to endure many rounds of extensive and exhausting chemotherapy that have a low chance of fully eliminating the tumor. 

Conventional surgery techniques are also ineffective--at a certain point in its growth, a glioma will have buried and anchored itself so securely to the surrounding tissue that it cannot be fully removed and will simply regenerate from the cells left behind after surgery. A patient may have to undergo many subsequent surgeries if the initial one is unsuccessful. Due to these factors, the mortality rate for those affected by glioma is high.

Because the typical treatment for glioma is both harsh and rarely successful, scientists and researchers have been looking for alternatives for several years now. The project we helped collect data for focused on the general goal of inducing genetic change using principles of biochemistry in order to create a gentler and more successful form of therapy. From reading up on previous studies (which our lab mentor insisted we also read when we weren't working), our lab mentor picked a specific kind of genetic material named microRNA-145 to test with.

Here is a picture of the distinct components of microRNA-145.

Our research showed that increasing the amount of microRNA-145 near the glioma can almost completely stop growth of the glioma if the increase is induced soon enough. This does not, however, mean that this mechanism doesn't work for glioma that is in a later stage of growth. Increasing the amount of microRNA-145 can halt the invasion or spread and movement of the tumor into neighboring brain or spinal tissue. While not necessarily a full cure for glioma quite yet, it is nevertheless promising.

Genetic engineering, however, is not limited to just medical innovation. In fact, the practice is much older and the developments I have discussed in this post are relatively recent--less than five years old. Frederick Griffith established the foundation for genetic engineering with experiments in 1928 that helped us understand the basic nature of genes and DNA. Since its potential was discovered, genetic engineering has made many other important breakthroughs such as the "Flavr-Savr" tomato (a tomato designed to remain ripe longer) in 1987.

Many of the tomatoes that we eat today are designed to remain fresh longer using modified versions of the techniques originally developed by researchers at Calgene in 1987. We come into contact with genetic engineering daily!

In the last decade however, genetic research has helped spur more medical innovation than anything else. Research into this specific kind of genetic engineering (controlling the amount of product a certain microRNA is yielding) has yielded fruitful results. Aside from cancer therapy, this method of genetic engineering has also been proven to be successful in treating genetic diseases such as Feingold syndrome. It has also determined a possible cause of hereditary cardiovascular disease that causes abnormal enlargement of the heart and fatal clotting. Research is currently under way to see if this knowledge can be used to formulate a cure for the disease itself. Based on its current trajectory, genetic engineering promises to have many positive benefits in the future.

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I am currently a senior at DCDS planning to study public health and international relations in college with aspirations to become a doctor.

Marijuana: Keep it Clean

Most people find it hard to regard any business and any professional who deals with marijuana as legitimate. But it’s not fair. Because for the thousands of people in the U.S. that rely on cannabis to treat symptoms ranging from nausea to chronic seizures, the marijuana industry is oftentimes a last hope for treatment. The taboo that we place on marijuana, medical or not, has a very real impact on the quality of the treatment that these patients are able to get. Instead of being able to trust the drug like you and I could trust an ibuprofen pill, medical marijuana patients usually do not know how strong their dosage is and also risk consuming a wide range of contaminants along with their treatment. The pressure that results from the prevailing negative view of the drug scares away chemists needed to test marijuana and prevents most medical marijuana dispensaries from even having a quality control facility to rely on.

The availability of marijuana for both medicinal and recreational purposes is rapidly increasing in America. 20 states and D.C. have legalized medical marijuana, and you probably remember Washington and Colorado approving recreational use of the drug over a year ago. Of course, testing labs have not been able to keep pace, and dispensaries across the country have no choice but to sell untested and unregulated marijuana.

Quality control labs, as a part of the marijuana industry, serve a two-fold purpose when testing product. They first measure potency with a technique called high-performance liquid chromatography (HPLC) in order to determine the amount of active ingredient present in a certain batch of marijuana. The main source of the effects of marijuana is tetrahydrocannabinol (THC), but no dose of the drug has the exact same amount. People often report getting too much or too little of the desired effects from a prescribed measure, either freaking them out with the intense psychoactive reactions or failing to fully cure their symptoms.

In addition to potency testing, these labs also conduct safety tests to ensure that sold marijuana will not contain traces of dangerous compounds like pesticides, mold, and microbes such as E.Coli and Salmonella. Gas chromatography (GC) is a popular method used in labs to test for any contaminants and, when combined with mass spectrometry, reveals the composition of chemicals in a sample of marijuana.

Labs still have a ways to go in developing new methods to test potency and safety, however. A sample of marijuana can contain a carboxylated form of THC called THC-acid, and when put through GC, the THC-acid decarboxylates to become regular THC. This inflates the potency reading of the sample and, in the end, gives the patient a smaller dose of the drug than he or she would need. Imagine taking a prescribed amount of cold medicine, let’s say, but never getting the relief you paid for because the medicine was not thoroughly tested. This is the reality that marijuana patients often face when they seek treatment.

There is a real market, with a real supply and demand, in marijuana. And if we’re talking about medical marijuana, then there is a real need for the product too. Yet, testing labs have not received the support they need to keep up with the ever-increasing number of people that can now legally buy cannabis. We’ve already allowed marijuana use to grow past a point of no return, so it’s time that we recognize and start respecting the drug for what it is: an industry. By casting off our childish aversion to cannabis and allowing testing centers to ensure the safety of this industry’s product, we can give medical marijuana patients a fair chance at treatment.

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I feel the need to state that I, personally, do not support marijuana use other than for necessary medical treatment. It’s a moral issue.

All seriousness aside, I'm Zack, a high school senior interested in studying Political Science next year who loves to run and swim.

Seitan: Really That Bad?

Driving down the street in the cold winter months, I am constantly confronted and begrudgingly badgered with signs for Big Macs, Whoppers, and supersized meals. In a world that often preaches going green and eating healthy, the constant barrage of advertising promotes the opposite in an effort to draw me into an establishment, serving unhealthy meals made with nothing more than grease and grimy grills.

When I think about the alternatives and what it means to eat a healthy diet, I am reminded of my oldest sister who is a self-proclaimed vegetarian or vegan or Vulcan (just kidding sis!) or whatever they call themselves nowadays. I respect her for her decisions but I get a bit annoyed every time I see her as she tries to convince me and my other family members, to no avail, to become vegan. I have tried several of the various dishes and while she makes some that I do like, I don’t like them enough to give up my regular diet!

Just as she believes there is only one way to be healthy, I am concerned with some of the food choices and the limitations of a vegan diet. With that in mind, I took it upon myself to do a little bit of research into protein substitutes that are similar to that of meat in both taste and texture. I am not referring to the butt of many Thanksgiving jokes, the proverbial Tofurkey, but something that I would consider a reasonable alternative if I were to actually try a similar vegan diet. My research lead me to a recent article found in the Chemical and Engineering News Magazine on a truly natural and healthy alternative to meat. Seitan, also known as wheat meat, fu, mock duck, and wheat gluten, is made from a doughy material, consisting of wheat flour and water. The wheat dough can be kneaded and molded to form a protein-loaded, meat-like mass that can very accurately mimic the texture and taste of several different meats, in particular chicken.

I’m not sure if my sister would even try Seitan because it can be prepared in such a manner that it actually looks and tastes like chicken. That alone would be a big barrier to overcome for someone who has been vegan as long as she has. Still, I am going to experiment with the process of making Seitan. I find the chemistry behind the process just as interesting as attempting to create the perfect mock duck or chicken as described in the various articles I read.

The aforementioned article detailed a journal found in the Journal of the Academy of Nutrition and Dietetics that outlines the benefits of a wheat-filled (more specifically gluten-filled) diet. Seitan is made up of two important proteins needed for gluten formation called gliadins and glutenins, the wheat meat is truly rich in essential nutrients. What was particularly interesting for me was discovering the benefits of this gluten-based food. The wheat meat, through oligofructose and inulin (starches found in gluten), creates a varied composition of colon bacteria which help to prevent many diseases and ailments. Studies show that these gluten-created and gluten-reinforced bacteria are able to protect against certain cancers, inflammatory conditions, and vascular problems found in the digestive tract. Gliadin positively impacts the body in other ways, as well; it can help to regulate both blood pressure and immune function.

The benefits of the wheat meat are many, providing a truly healthy and nutritious substitute for meat. Maybe by the time I am done with my Seitan experiment, I will be able to come up with something that will be both healthy and satisfying for the vegans (my sister’s husband is also vegan) and the rest of my family as well.

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Danny: I am a high school student, football player, lacrosse player, drummer, and an Eagle Scout. I’ve never blogged before, but I hope you enjoy my post! 

Umami Bomb

Why do people like Chinese food? Is it because of the General Tao’s Chicken, the fried egg rolls, the novelty of using chopsticks, or the fortune cookies filled with vague yet forever optimistic fortunes?

The answer lies in the magical properties of soy sauce. Unbeknownst to many, this signature component of Chinese cooking is made of fermented bean paste. Although fermented bean paste sounds disgusting, many people’s taste buds find it absolutely delightful because it contains Monosodium Glutamate or MSG. MSG, a synthesized form of the amino acid glutamate, is the fairy dust that makes food more appetizing by producing an umami flavor.

The most recently discovered of the five basic flavors, umami means “deliciousness” in Japanese. Just from the name, you can tell this flavor is really tasty. Researchers have gone crazy trying to learn more about this new flavor and how it influences our eating behavior. Even before the discovery of umami, people have been unknowingly attracted to its flavor. The classic pairing of cheese on marinara sauce is so successful because both cheese and tomatoes naturally contain glutamate. Together they form what the food industry calls an umami bomb, basically a party for your taste buds.

In this research paper published by the Journal of Nutrition & Food Sciences in 2012, these

four scientists found that not only are there glutamate receptors in the tongue, there are also glutamate receptors in the stomach. The stomach can also sense the other 19 amino acids, but it is most sensitive to glutamate. How crazy is that? Your stomach can taste glutamate!

The paper also found that eating glutamate increased protein digestion and protein absorption leading people to feel fuller. When I read this, I was so surprised. Glutamate is supposed to make me full, but why do I finish a bag of Doritos and then automatically reach for another one? I don’t know the answer, but food brands are taking advantage of this addictive nature of umami. By using ingredients that naturally contain glutamate, food companies are trying to incorporate the umami flavor into their food products.

At home, I am rarely exposed to MSG because my mom thinks it has negative effects on the body. She prefers to use fresh ingredients and I actually enjoy her cooking, much to her pleasure. While my mom doesn’t use MSG, Chinese restaurants are not at all hesitant to add MSG, because MSG is a cheap flavor enhancer that gives food an extra boost of flavor. Eating MSG loaded food once in a while is not too bad, but after eating too much MSG, I always feel nauseous. Perhaps, instead of using synthetic glutamate, use ingredients that naturally contain glutamate to make an umami bomb. 

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I’m a high school senior who wants to enjoy all the world has to offer, especially the food.